NEWS
The newly-founded Misfolding Club at Umeå University unites scientists studying different diseases caused by misfolded proteins. The long-term goal is to cultivate a fertile scientific environment.
Ten or so research groups from a range of disciplines are now joining forces to investigate the mysteries surrounding misfolded proteins and the diseases they cause. The initiative kicked off in January with a “mini symposium,” arranged to showcase the University’s wide range of expertise on the subject. Since then, the Misfolding Club has met once a month.
Fredrik Almqvist, Professor of organic chemistry, is one of the initiators: “It’s wonderful to see that so many young, competent scientists join the group. And we have an incredible span of know-how, ranging from molecular biology, chemistry and fruit fly research and crystallography to a clinical approach.”
One of the young, promising scientists from the Club, Magnus Wolf-Watz, was recently honored by The Royal Skytte Society for his studies on the mechanisms connected to enzyme mobility and function.
The hope is that these meetings will establish a scientific environment where scientists can see the end results of their studies, and where younger researchers get a chance to cooperate in their day-to-day work. In the long run the Misfolding Club is designed to create a breeding ground for a new strong research environment to flourish at the university. The imminent recruitment of the highly merited Pernilla Wittung-Stafshede from Rice University, Texas, will add even more strength to the cooperation.
“Pernilla slots perfectly into our project. Once she’s a part of the team we will start to apply for larger common research grants. Then we’ll be comprehensive enough to apply for more substantial research grants,” states Fredrik Almqvist.
Difficult to define
Fredrik emphasizes that the Club’s research areas not only cover prions and amyloid creation, which among other things causes Alzheimer’s disease and FAP, familiar amyloidosis with polyneuropathy. But the research also encompasses the misfolding of non-aggregating proteins, such as in the case of ALS.
Defining misfolding is not the easiest of tasks, but one might say that a protein is misfolded when it produces an undesired biological effect. Misfolded proteins affect all organisms that possess a system that deals with proteins that are not folded correctly.
“That way bacteria can prove to be a good model when looking at amyloid diseases. Here in Umeå we also have a very interesting model involving fruit flies that develop FAP,” explains Fredrik Almqvist.
There are also a number of interesting theories about connections between bacterial infections and misfolding diseases. Today we know that bacteria can create fibre-like structures, which can then induce amyloid formation, explains Fredrik and predicts a larger overlap between infection and misfolding researchers in the future.
